Molecules and Cells

Indexed in /covered by CAS, KoreaScience & DOI/Crossref:eISSN 0219-1032   pISSN 1016-8478

Fig. 1.

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Fig. 1. Composition of Hda1C and its role in transcription. (A) Hda1C is a class II HDAC identified in yeast and is composed of a Hda1 homodimer and Hda2-3 heterodimer. Hda1 is the catalytic subunit and both Hda2 and Hda3 are essential for the HDAC activity of Hda1C. (B) Hda1 has a HDAC domain and an Arb2 domain at its N-terminus and C-terminus, respectively. Although the Arb2 domain directly interacts with histone octamers in vitro, its function in vivo remains unknown. Both Hda2 and Hda3 show sequence similarity and have a potential DNA binding domain and a coiled-coil domain at their N- and C-terminal regions, respectively. The HDAC domain of Hda1 and coiled-coil domains of Hda2 and Hda3 directly interact to form a stable complex. (C) Hda1C deacetylates histone H3 and H2B to repress transcription. Hda1C is recruited to stress response genes via gene-specific repressors and a general corepressor, Tup1, and selectively deacetylates histone H3 and H2B to repress RNA Pol II transcription.
Mol. Cells 2020;43:841~847
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